Naslov
The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron

Autori
Tomin, Marko ; Tomić, Antonija ; Kovačević, Borislav ; Tomić, Sanja

Izvornik
Croatica chemica acta (0011-1643) 91 (2018), 2; 187-193

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
dipeptidyl peptidase III ; DPP III ; peptide hydrolysis ; reaction mechanism ; Bacteroides thetaiotaomicron

Sažetak
Dipeptidyl peptidase III (DPP III) is a zinc- dependent peptidase that cleaves dipeptides off of N-termini of its substrates. Previous studies on human DPP III reveal a reaction mechanism similar to that of thermolysin. Since the active site is conserved within the DPP III family, it is not surprising that the mechanism determined for Bacteroides thetaiotaomicron DPP III (BtDPP III) closely resembles that of hDPP III. However, the hydrogen bond network within the model differs slightly from that in the human ortholog, which results in two proposed pathways. The calculated Gibbs activation energy of 90.1 kJ mol–1 is larger than the one calculated from kinetic data for the preferred substrate Arg2-2-naphthylamide at room temperature (69 kJ mol–1), suggesting the importance of treating the whole DPP III enzyme in the calculations.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

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